KEGG   ENZYME: 1.1.1.282
Entry
EC 1.1.1.282                Enzyme                                 

Name
quinate/shikimate dehydrogenase [NAD(P)+];
YdiB;
quinate/shikimate dehydrogenase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-quinate:NAD(P)+ 3-oxidoreductase
Reaction(IUBMB)
(1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ [RN:R01872 R06846];
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ [RN:R02413 R06847]
Reaction(KEGG)
Substrate
L-quinate [CPD:C00296];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
shikimate [CPD:C00493]
Product
3-dehydroquinate [CPD:C00944];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
3-dehydroshikimate [CPD:C02637]
Comment
This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
History
EC 1.1.1.282 created 2004, modified 2021
Pathway
ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K05887  quinate/shikimate dehydrogenase
Genes
ECO: b1692(ydiB)
ECJ: JW1682(ydiB)
ECD: ECDH10B_1828(ydiB)
EBW: BWG_1506(ydiB)
ECOK: ECMDS42_1365(ydiB)
ECE: Z2720(ydiB)
ECS: ECs2399(aroE)
ECF: ECH74115_2408
ETW: ECSP_2259(ydiB)
ELX: CDCO157_2233(aroE)
EOI: ECO111_2161(ydiB)
EOJ: ECO26_2420(ydiB)
EOH: ECO103_1835(ydiB)
ECOO: ECRM13514_2187(aroE)
ECOH: ECRM13516_2092(aroE)
ESL: O3K_11775
ESO: O3O_13860
ESM: O3M_11740
ECK: EC55989_1859(ydiB)
ECG: E2348C_1777(ydiB)
EOK: G2583_2089(ydiB)
ELH: ETEC_1725
ECP: ECP_1639
ENA: ECNA114_1739(ydiB)
ECOS: EC958_1912(ydiB)
ECV: APECO1_768(ydiB)
ECY: ECSE_1815
ECR: ECIAI1_1745(ydiB)
ECQ: ECED1_1891(ydiB)
EUM: ECUMN_1981(ydiB)
ECT: ECIAI39_1366(ydiB)
EOC: CE10_1966(ydiB)
EBR: ECB_01661(ydiB)
EBL: ECD_01661(ydiB)
EBE: B21_01650(ydiB)
EBD: ECBD_1954
ECI: UTI89_C1884(ydiB)
ECZ: ECS88_1742(ydiB)
ECC: c2087(ydiB)
ESE: ECSF_1552
EKF: KO11_14285(ydiB)
EAB: ECABU_c19460(ydiB)
EDJ: ECDH1ME8569_1636(ydiB)
ELW: ECW_m1861(ydiB)
ELL: WFL_09110(ydiB)
ELC: i14_1909(aroE)
ELD: i02_1909(aroE)
ELP: P12B_c1391(aroE)
ELF: LF82_2870(ydiB)
ECOI: ECOPMV1_01791(ydiB)
ECOJ: P423_09035
EFE: EFER_0091
ESZ: FEM44_23400(ydiB)
STM: STM1359(ydiB)
SEO: STM14_1650(aroE_1)
SEY: SL1344_1293(aroE)
SEJ: STMUK_1326(aroE)
SEB: STM474_1364(aroE)
SEF: UMN798_1416(aroE)
SENR: STMDT2_12921(aroE)
SEND: DT104_13371(aroE)
SENI: CY43_06920
SEI: SPC_2371(aroE)
SEC: SCH_1378(ydiB)
SHB: SU5_01977
SENS: Q786_08455
SED: SeD_A1984
SEG: SG1757(ydiB)
SEL: SPUL_1177(ydiB)
SEGA: SPUCDC_1177(ydiB)
SET: SEN1685(ydiB)
SENA: AU38_08725
SENO: AU37_08730
SENV: AU39_08735
SENQ: AU40_09735
SENL: IY59_08920
SEEP: I137_05420
SENE: IA1_06705
SFL: SF1722(aroE)
SFX: S1854(ydiB)
SFV: SFV_1718(ydiB)
SFE: SFxv_1929(ydiB)
SFN: SFy_2467
SFS: SFyv_2522
SFT: NCTC1_01868(ydiB)
SSN: SSON_1462(ydiB)
SDY: SDY_1475(ydiB)
ENF: AKI40_1900(ydiB)
KPU: KP1_0890(aroE)
KPP: A79E_4226
KPT: VK055_2498(ydiB)
KPO: KPN2242_02810(aroE)
KPR: KPR_0998
KPJ: N559_4356
KPX: PMK1_02383(aroE_2)
KPNU: LI86_22370
KPNK: BN49_4265
KVA: Kvar_4308
KPE: KPK_4667
KOX: KOX_10830(aroE)
KOE: A225_0875
KOY: J415_26885(aroE)
EAE: EAE_11160(aroE)
EAR: CCG31755
CPOT: FOB25_01110(ydiB)
CAMA: F384_06180
CTEL: GBC03_18520(ydiB)
CITZ: E4Z61_03985(ydiB)
METY: MRY16398_47470(aroE)
SUTK: FG381_00155(ydiB)
SWS: I6J16_03205(ydiB)
BAQ: BACAU_0778(aroE1)
BYA: BANAU_0723(aroE1)
BAMP: B938_03870
BAMA: RBAU_0782(ydiB)
BAMN: BASU_0758(ydiB)
BAMB: BAPNAU_0734(aroE1)
BAMT: AJ82_04495
BAMY: V529_07450
BMP: NG74_00799(aroE_1)
BAO: BAMF_0755(RBAM_008070)
BQL: LL3_00809
BQY: MUS_0802(aroE)
BAMI: KSO_015775
BAMC: U471_07900
BAMF: U722_04025
BACI: B1NLA3E_05085(aroE) B1NLA3E_05110(aroE)
BACP: SB24_05875
BACB: OY17_06660
BMQ: BMQ_0974(aroD)
BMD: BMD_0975(aroD) BMD_3610
BMEG: BG04_3263(aroE) BG04_523
LMOE: BN418_0563
LMOB: BN419_0569
LIV: LIV_2223
PPY: PPE_00893
PPM: PPSC2_04635(ydiB1)
PPO: PPM_0869(ydiB1)
PPOL: X809_04280
PPQ: PPSQR21_009250(aroE)
PPOY: RE92_07330
LCA: LSEI_0476
LCS: LCBD_0541(aroDE)
LCE: LC2W_0542(aroDE)
LCW: BN194_05480(aroE_2)
LPAP: LBPC_0442
LPJ: JDM1_2789(aroD3) JDM1_2790(aroD4)
LPT: zj316_0126(aroD3) zj316_0127(aroD4)
ECAS: ECBG_02583
EDU: LIU_07945
EGA: AL523_01565(aroE)
JAR: G7057_00650(aroE)
CKL: CKL_1014(aroE3)
CKR: CKR_0918
CSB: CLSA_c07000(aroE2) CLSA_c07040(aroE3)
CSQ: CSCA_1647
RUM: CK1_34250
OVA: OBV_35430(aroE)
BFI: CIY_16020
RIX: RO1_38400
RIM: ROI_16940
CCT: CC1_23550
BLAB: EYS05_11210(aroE)
CSCI: HDCHBGLK_02860(aroE)
EHL: EHLA_0534
RTO: RTO_32440
ERT: EUR_24270
ERA: ERE_09960
PDC: CDIF630_02965(aroE2)
CDC: CD196_2549(ydiB)
CDL: CDR20291_2596(ydiB)
PDF: CD630DERM_27080(aroE2)
ELM: ELI_0966
BPRS: CK3_17120
EBM: SG0102_23460(aroE)
TPYO: X956_05370
ELE: Elen_2551
XII: AMD24_00667(ydiB)
 » show all
Reference
1  [PMID:12637497]
  Authors
Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ
  Title
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
  Journal
J Biol Chem 278:19463-72 (2003)
DOI:10.1074/jbc.M300794200
  Sequence
[eco:b1692]
Reference
2  [PMID:12624088]
  Authors
Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF.
  Title
The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
  Journal
J Biol Chem 278:19176-82 (2003)
DOI:10.1074/jbc.M301348200
  Sequence
[eco:b1692]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.282
IUBMB Enzyme Nomenclature: 1.1.1.282
ExPASy - ENZYME nomenclature database: 1.1.1.282
BRENDA, the Enzyme Database: 1.1.1.282

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